ID   SDHD_ALKHC              Reviewed;         442 AA.
AC   Q9KC12;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable D-serine dehydratase {ECO:0000255|HAMAP-Rule:MF_01030};
DE            EC=4.3.1.18 {ECO:0000255|HAMAP-Rule:MF_01030};
DE   AltName: Full=D-serine deaminase {ECO:0000255|HAMAP-Rule:MF_01030};
DE            Short=DSD {ECO:0000255|HAMAP-Rule:MF_01030};
GN   Name=dsdA {ECO:0000255|HAMAP-Rule:MF_01030}; OrderedLocusNames=BH1762;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01030}.
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DR   EMBL; BA000004; BAB05481.1; -; Genomic_DNA.
DR   PIR; B83870; B83870.
DR   RefSeq; WP_010897923.1; NC_002570.2.
DR   AlphaFoldDB; Q9KC12; -.
DR   SMR; Q9KC12; -.
DR   STRING; 272558.10174380; -.
DR   EnsemblBacteria; BAB05481; BAB05481; BAB05481.
DR   KEGG; bha:BH1762; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_9; -.
DR   OMA; ESDPNCF; -.
DR   OrthoDB; 912282at2; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0046416; P:D-amino acid metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_01030; D_Ser_dehydrat; 1.
DR   InterPro; IPR011780; D_Ser_am_lyase.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   PANTHER; PTHR48078:SF9; PTHR48078:SF9; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR02035; D_Ser_am_lyase; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..442
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000185604"
FT   MOD_RES         115
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   442 AA;  49152 MW;  78EFA507B368BC9E CRC64;
     MNELEQWRKD PLVIKLMATE EVFWLNPHID SFKSAVRKLS LHEDDVKDAE KRLDRFAPYI
     AKVFPGTNQA HGMIESPLVQ IPSMKQSLEQ KYLQPITGNL LLKCDSHLPI SGSIKARGGI
     YEVLKHAEQL ALQHGLLTVQ DDYSILDSET CRDFFANYSI AVGSTGNLGL SIGIISAKLG
     FNVSVHMSAD AKQWKKDLLR SKNVNVIEYE DDYSQAVEEG RREAEQDPTC YFVDDEQSQD
     LFLGYAVAAF RLKKQLAEQK ITVDESHPLF VYLPCGVGGA PGGITFGLKL LFEDHVHCFF
     AEPTHSPSML LGLLTGLHER ISVQEIGLDN RTEADGLAVG RPSRLVSRLM KPLLSGSFTI
     DDDKLFTLLK ELADAEGLFL EPSALAGMLG PIKLVQEGNH YLKANNLAEK MNNATHIIWG
     TGGSMVPEEE MMAYYRRGGT IK